Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis

Microsomal glutathione S-transferase 2 (MGST2) produces leukotriene C4, an intracrine mediator of cell death. Structural, biochemical and computational analyses of human MGST2 suggest a mechanism employed by the enzyme to restrict catalysis to only one active site within the MGST2 trimer.

Bibliographic Details
Main Authors: Madhuranayaki Thulasingam, Laura Orellana, Emmanuel Nji, Shabbir Ahmad, Agnes Rinaldo-Matthis, Jesper Z. Haeggström
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21924-8
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spelling doaj-ad8bc33695d24df2a94e100658df694b2021-03-21T12:13:23ZengNature Publishing GroupNature Communications2041-17232021-03-0112111210.1038/s41467-021-21924-8Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysisMadhuranayaki Thulasingam0Laura Orellana1Emmanuel Nji2Shabbir Ahmad3Agnes Rinaldo-Matthis4Jesper Z. Haeggström5Department of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska InstitutetDepartment of Biochemistry and Biophysics, Stockholm UniversityDepartment of Biochemistry and Biophysics, Stockholm UniversityDepartment of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska InstitutetDepartment of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska InstitutetDepartment of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska InstitutetMicrosomal glutathione S-transferase 2 (MGST2) produces leukotriene C4, an intracrine mediator of cell death. Structural, biochemical and computational analyses of human MGST2 suggest a mechanism employed by the enzyme to restrict catalysis to only one active site within the MGST2 trimer.https://doi.org/10.1038/s41467-021-21924-8
collection DOAJ
language English
format Article
sources DOAJ
author Madhuranayaki Thulasingam
Laura Orellana
Emmanuel Nji
Shabbir Ahmad
Agnes Rinaldo-Matthis
Jesper Z. Haeggström
spellingShingle Madhuranayaki Thulasingam
Laura Orellana
Emmanuel Nji
Shabbir Ahmad
Agnes Rinaldo-Matthis
Jesper Z. Haeggström
Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
Nature Communications
author_facet Madhuranayaki Thulasingam
Laura Orellana
Emmanuel Nji
Shabbir Ahmad
Agnes Rinaldo-Matthis
Jesper Z. Haeggström
author_sort Madhuranayaki Thulasingam
title Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
title_short Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
title_full Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
title_fullStr Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
title_full_unstemmed Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
title_sort crystal structures of human mgst2 reveal synchronized conformational changes regulating catalysis
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-03-01
description Microsomal glutathione S-transferase 2 (MGST2) produces leukotriene C4, an intracrine mediator of cell death. Structural, biochemical and computational analyses of human MGST2 suggest a mechanism employed by the enzyme to restrict catalysis to only one active site within the MGST2 trimer.
url https://doi.org/10.1038/s41467-021-21924-8
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